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Cav3 is involved in muscle development and is required for correct intracellular organization and myoblast fusion.
The caveolin 3 G56S variant is not a clearly pathogenic mutation, but may influence cellular functions and morphologies resulting in an increased cellular vulnerability in terms of a modifying factor.
Our results indicate that HCN4 (show HCN4 ELISA Kits) channel function is modulated by cav-3. LQTS-associated mutations of cav-3 differentially influence pacemaker current properties indicating a pathophysiological role in clinical manifestations.
This study demonstrated that the Caveolin-3 is aberrantly expressed in skeletal muscle cells in myasthenia gravis.
Study characterized the secondary structure, dynamics, and topology of a lipidated full-length human Cav3 construct, demonstrated that the N-terminal domain undergoes a dramatic topological rearrangement in both micelles and vesicles that is reversibly mediated by pH
The Cav3 P104L mutation of limb girdle muscular dystrophy-1C leads to disordered glucose metabolism in muscle cells.
Data (including data from studies using recombinant proteins that lack typical in-vivo post-translational modifications such as palmitoylation) suggest Cav3 exhibits little tendency to partition into liquid-ordered domains of unilamellar vesicles.
MURC/cavin-4 (show MURC ELISA Kits), especially in combination with Cav-3, may play a consistent role in the differentiation process of rhabdomyosarcoma.
This study demonstrated that cav3 mutation in stinct disorders including limb-girdle muscular dystrophy 1C, rippling muscle disease, and isolated creatine kinase elevation in Greece.
In a nonreferred nationwide Danish cohort of SIDS (show IDS ELISA Kits) cases, up to 5/66 (7.5%) of SIDS (show IDS ELISA Kits) cases can be explained by genetic variants in the sodium channel complex genes.
our results indicate that inhibition of Cav3 currents by 5,6-epoxyeicosatrienoic acid is an important mechanism controlling the vascular tone.
Data show that caveolin-3 binds to low glycosylated extracellular matrix metalloproteinase inducer (LG-EMMPRIN) in cardiac cells and in the hearts of healthy mice.
Cav-3 overexpressing mice have changes in ECG intervals, heart rates, and cardiac ion channel expression
Loss of CAV3 interferes with downstream insulin (show INS ELISA Kits) signaling and lipid uptake and increases susceptibility to palmitate-induced insulin (show INS ELISA Kits) resistance.
eNOS (show NOS3 ELISA Kits), caveolin-3, and connexin-43 (show GJA1 ELISA Kits) were detected in subsarcolemmal mitochondria
Data show increased expression of T-type Ca(2 (show CA2 ELISA Kits)+) current and association of protein kinase C alpha (PKCalpha (show PKCa ELISA Kits)) with caveolin-3 (Cav-3)was disrupted in the hypertrophic ventricular myocyte.
Cardioprotection in myocardial infarction is abolished in caveolin-3 knockout mice.
The lithogenic diet was associated with significantly lower CAV3 in the liver and lower CAV3 and CCKAR (show CCKAR ELISA Kits) in the gallbladder compared with the control mice.
Cav-3 may be a novel participant in B-cell expression, T-cell cytokine production and activation of inflammation
Cav3 protein can modify integrin function and mechanotransduction in the cardiomyocyte and intact heart
cloned and characterized caveolin-3 from porcine muscle; caveolin-3 was expressed specifically in skeletal muscle & heart; first evidence that caveolin-3 has a certain regulated expression pattern during the prenatal period of skeletal muscle development
This gene encodes a caveolin family member, which functions as a component of the caveolae plasma membranes found in most cell types. Caveolin proteins are proposed to be scaffolding proteins for organizing and concentrating certain caveolin-interacting molecules. Mutations identified in this gene lead to interference with protein oligomerization or intra-cellular routing, disrupting caveolae formation and resulting in Limb-Girdle muscular dystrophy type-1C (LGMD-1C), hyperCKemia or rippling muscle disease (RMD). Alternative splicing has been identified for this locus, with inclusion or exclusion of a differentially spliced intron. In addition, transcripts utilize multiple polyA sites and contain two potential translation initiation sites.
, calveolin 3
, caveolin 3